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. 2017 Dec 11;7:17332. doi: 10.1038/s41598-017-17427-6

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© The Author(s) 2017

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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The active components inhibit the activity of RANKL-induced osteoclasts. BMMs were seeded onto Osteo Assay Surface Plates and incubated in α-MEM containing M-CSF (30 ng/mL) and RANKL (100 ng/mL) for 5 days. The cells were then exposed to the indicated concentrations of artemisinin (ART), artemisinic acid (AA), or arteannuin B (AB) for an additional 2 days. (a) The cells were lysed with 5% sodium hypochlorite solution, and the formed resorption pits were examined using light microscopy (magnification, ×100). The resorbed area was calculated using ImageJ software. (b) MMP-2 and MMP-9 activities and (c) cathepsin K activity were detected using gelatin zymography and a commercially available cathepsin K assay kit. The images are representative, and the data are expressed as the mean ± SE of triplicate experiments. ^# P < 0.01 versus BMMs without RANKL (C), ^* P < 0.05, ^** P < 0.01 versus BMMs with RANKL alone.